1osg: Difference between revisions

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[[Image:1osg.gif|left|200px]]<br /><applet load="1osg" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1osg.gif|left|200px]]
caption="1osg, resolution 3.00&Aring;" />
 
'''Complex between BAFF and a BR3 derived peptide presented in a beta-hairpin scaffold'''<br />
{{Structure
|PDB= 1osg |SIZE=350|CAPTION= <scene name='initialview01'>1osg</scene>, resolution 3.00&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
|ACTIVITY=
|GENE= BAFF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
}}
 
'''Complex between BAFF and a BR3 derived peptide presented in a beta-hairpin scaffold'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1OSG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OSG OCA].  
1OSG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OSG OCA].  


==Reference==
==Reference==
BAFF/BLyS receptor 3 comprises a minimal TNF receptor-like module that encodes a highly focused ligand-binding site., Gordon NC, Pan B, Hymowitz SG, Yin J, Kelley RF, Cochran AG, Yan M, Dixit VM, Fairbrother WJ, Starovasnik MA, Biochemistry. 2003 May 27;42(20):5977-83. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12755599 12755599]
BAFF/BLyS receptor 3 comprises a minimal TNF receptor-like module that encodes a highly focused ligand-binding site., Gordon NC, Pan B, Hymowitz SG, Yin J, Kelley RF, Cochran AG, Yan M, Dixit VM, Fairbrother WJ, Starovasnik MA, Biochemistry. 2003 May 27;42(20):5977-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12755599 12755599]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: protein-peptide complex]]
[[Category: protein-peptide complex]]


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Revision as of 14:15, 20 March 2008

File:1osg.gif


PDB ID 1osg

Drag the structure with the mouse to rotate
, resolution 3.00Å
Ligands:
Gene: BAFF (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



Complex between BAFF and a BR3 derived peptide presented in a beta-hairpin scaffold


OverviewOverview

BAFF/BLyS, a member of the tumor necrosis family (TNF) superfamily of ligands, is a crucial survival factor for B cells. BAFF binds three receptors, TACI, BCMA, and BR3, with signaling through BR3 being essential for promoting B cell function. Typical TNF receptor (TNFR) family members bind their cognate ligands through interactions with two cysteine-rich domains (CRDs). However, the extracellular domain (ECD) of BR3 consists of only a partial CRD, with cysteine spacing distinct from other modules described previously. Herein, we report the solution structure of the BR3 ECD. A core region of only 19 residues adopts a stable structure in solution. The BR3 fold is analogous to the first half of a canonical TNFR CRD but is stabilized by an additional noncanonical disulfide bond. BAFF-binding determinants were identified by shotgun alanine-scanning mutagenesis of the BR3 ECD expressed on phage. Several of the key BAFF-binding residues are presented from a beta-turn that we have shown previously to be sufficient for ligand binding when transferred to a structured beta-hairpin scaffold [Kayagaki, N., Yan, M., Seshasayee, D., Wang, H., Lee, W., French, D. M., Grewal, I. S., Cochran, A. G., Gordon, N. C., Yin, J., Starovasnik, M. A, and Dixit, V. M. (2002) Immunity 10, 515-524]. Outside of the turn, mutagenesis identifies additional hydrophobic contacts that enhance the BAFF-BR3 interaction. The crystal structure of the minimal hairpin peptide, bhpBR3, in complex with BAFF reveals intimate packing of the six-residue BR3 turn into a cavity on the ligand surface. Thus, BR3 binds BAFF through a highly focused interaction site, unprecedented in the TNFR family.

About this StructureAbout this Structure

1OSG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

BAFF/BLyS receptor 3 comprises a minimal TNF receptor-like module that encodes a highly focused ligand-binding site., Gordon NC, Pan B, Hymowitz SG, Yin J, Kelley RF, Cochran AG, Yan M, Dixit VM, Fairbrother WJ, Starovasnik MA, Biochemistry. 2003 May 27;42(20):5977-83. PMID:12755599

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